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Team:Imperial College London/PPS
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To enable <b><i>The E.ncapsulator</i></b> to produce peptides without inhibiting their functionality, we have developed a removable linker region that starts with the amino acid methionine. Following the release of the peptide in the intestine, a naturally occuring enzyme (enteropeptidase) removes the linker region from the front of the peptide releasing the remainder in its functional form. The use of this linker region can be extended to any polypeptide that does not begin with methionine. | To enable <b><i>The E.ncapsulator</i></b> to produce peptides without inhibiting their functionality, we have developed a removable linker region that starts with the amino acid methionine. Following the release of the peptide in the intestine, a naturally occuring enzyme (enteropeptidase) removes the linker region from the front of the peptide releasing the remainder in its functional form. The use of this linker region can be extended to any polypeptide that does not begin with methionine. | ||
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Add instructions on attaching linker. | Add instructions on attaching linker. | ||
Revision as of 20:18, 17 September 2009
Peptide Processing
To enable The E.ncapsulator to produce peptides without inhibiting their functionality, we have developed a removable linker region that starts with the amino acid methionine. Following the release of the peptide in the intestine, a naturally occuring enzyme (enteropeptidase) removes the linker region from the front of the peptide releasing the remainder in its functional form. The use of this linker region can be extended to any polypeptide that does not begin with methionine.
Add instructions on attaching linker.
